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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Adsorption of the antimicrobial peptide tritrpticin onto solid and liquid surfaces: Ion-specific effects

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Author(s):
Salay, Luiz C. [1, 2] ; Petri, Denise F. S. [3] ; Nakaie, Clovis R. [4] ; Schreier, Shirley [1]
Total Authors: 4
Affiliation:
[1] Univ Sao Paulo, Inst Chem, Dept Biochem, Struct Biol Lab, BR-05513970 Sao Paulo - Brazil
[2] State Univ Santa Cruz UESC, Dept Exact Sci & Technol, Ilheus, BA - Brazil
[3] Univ Sao Paulo, Inst Chem, Dept Fundamental Chem, BR-05513970 Sao Paulo - Brazil
[4] Fed Univ Sao Paulo UNIFESP, Dept Biophys, BR-04044020 Sao Paulo - Brazil
Total Affiliations: 4
Document type: Journal article
Source: Biophysical Chemistry; v. 207, p. 128-134, DEC 2015.
Web of Science Citations: 6
Abstract

Developing functional biointerfaces is important for technological applications. We investigated the interaction and adsorption of the antimicrobial peptide tritrpticin (VRRFPWWWPFLRR, TRP3) onto solid and liquid surfaces and the influence of ions on these processes by several techniques. Surface tension measurements showed that salt addition to TRP3 solution causes a high decrease of surface tension due to the adsorption of TRP3 at air-liquid surface. Ellipsometry studies show the TRP3 adsorption on silicon surfaces forming nanometric films that are able to further interact with liposomes. Contact angle measurements gave insight on the nature of thin film and its roughness. AFM shows the topology of the film on the solid substrates. In addition, those techniques also showed that anions can act as modulators on adsorption phenomena and are correlated with the Hofmeister series. The findings of the current work are relevant for the development of functional interfaces such as biocidal surfaces. (C) 2015 Elsevier B.V. All rights reserved. (AU)